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Related Concept Videos

The Proteasome01:13

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
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The Proteasome02:18

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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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The Unfolded Protein Response01:37

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Regulation of the Unfolded Protein Response01:31

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Related Experiment Video

Updated: May 6, 2026

Detection of Inflammasome Activation and Pyroptotic Cell Death in Murine Bone Marrow-derived Macrophages
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Inflammasome activation by altered proteostasis.

Jin Na Shin1, Elmoataz Abdel Fattah, Abhisek Bhattacharya

  • 1From the Department of Medicine, Baylor College of Medicine, Houston, Texas 77030.

The Journal of Biological Chemistry
|November 2, 2013
PubMed
Summary
This summary is machine-generated.

Impaired protein homeostasis, or proteostasis, triggers inflammasome activation. This occurs through reactive oxygen species and lysosomal damage, linking proteostasis to inflammatory disorders.

Keywords:
AutophagyInflammasomeInflammationLysosomesMacrophagesProtein MisfoldingProteostasis

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Area of Science:

  • Molecular Biology
  • Immunology
  • Cell Biology

Background:

  • The link between disrupted proteostasis and inflammatory diseases is known, but mechanisms remain unclear.
  • Autophagy and sequestosome 1 (p62/SQSTM) are key proteostasis regulators.
  • Inflammasomes are critical mediators of inflammation.

Purpose of the Study:

  • To investigate the role of proteostasis in inflammasome activation.
  • To elucidate the mechanisms by which altered proteostasis leads to inflammation.

Main Methods:

  • Primary macrophage cultures and in vivo mouse models were used.
  • Inflammasome activation was assessed in response to lipopolysaccharide (LPS) and adenosine triphosphate (ATP).
  • Protein misfolding was induced using chemical agents (puromycin, thapsigargin, geldanamycin).

Main Results:

  • Autophagy or p62 deficiency caused inflammasome hyperactivation.
  • Protein misfolding exacerbated inflammasome activation, particularly in deficient cells.
  • Misfolded protein accumulation induced inflammasome activation via reactive oxygen species and lysosomal damage, releasing cathepsin B.

Conclusions:

  • Altered proteostasis directly results in inflammasome activation.
  • This study provides mechanistic insights into the connection between proteostasis and inflammatory disorders.
  • Targeting proteostasis pathways may offer therapeutic strategies for inflammatory conditions.